Hyperthermophilic proteins are often stabilized by increasing the pressure. This means that when pressure is increased, the folding free energy becomes more negative. What can you say about the density of the folded and unfolded states of these proteins?
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Hyperthermophilic proteins are often stabilized by increasing the pressure. This means that when pressure is increased, the folding free energy becomes more negative.
What can you say about the density of the folded and unfolded states of these proteins?
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- if i have protein with 110kda and its cysteine joining with disulfide bond . and one cysteine acids per 100 amino when i heated at 85c it lost activity but if i cool it the activity will restore the questions are : how many disulfide bonds in this protein with explanation? and what is molecular basis to restore activity?Amino acids are ionic compounds, very soluble in water. Proteins, however, which are made up of amino acids are much less soluble, and must be folded up very precisely to maximize their solubility. Why are proteins so much less soluble than the amino acids of which they are made?Globular proteins are typically constructed from several layers of secondary structure, with a hydrophobic core and a hydrophilic surface. Is this true for a fibrous protein such as keratin?
- The affinity of hemoglobin for oxygen varies according to the pH of the plasma. In fact, the warmer and more acidic your blood is, the more likely it is that hemoglobin will let go of oxygen. Explain, in terms of the secondary and tertiary structure of protein why this would be so.How much energy is released upon the hydrolysis of ATP? What happens to this energy during phosphate transfer to proteins? Given your answer, why is this significant? What is the consequence of this energy on the equilibrium constant for a conformational change of a protein?How does sickle cell hemoglobin differ from normal hemoglobin at the quaternary level of protein structure (the sum of all the folded protein chains)?
- You are given a protein solution with a concentration of 0.15 mg/ml. Suppose that we want to prepare a solution containing 100 μg of the protein at a concentration of 1 mg/ml. To achieve this, we will first dry down enough protein solution to obtain 100 μg of proteins. How much solution do we need for drying down? How much volume of H2O do we need to add to the dried protein to obtain the desired concentration?Most protein dissolve in neutral salt solution, is that true? Provide reasoningThe protein gamma globulin has an isoelectric point of 6.60. Suppose you did a pH titration of a solution containing gamma globulin. At what pH will the protein aggregate?
- a) Canonical forces in protein folding. Describe how these forces come into play when a protein folds. Why do are other intermolecular interactions important to fully understand folding processes?What type of protein is included in milk? When milk sourness occurs, why does this protein precipitate?Discuss the overall process or mechanisms that cause proteins to precipitate.What is the definition of amphoterism? Show the amphoteric property of protein using a chemical equation. Strictly no plagiarism. Please cite the references.You are given a pure protein sample to characterize and provided the following information: Its molar extinction coefficient, ε280, is 0.25 liters micromole-1 cm-1 in both the folded and unfolded form Its ΔGo for unfolding is 1.5 kcal/mol at 37o (where RT = 0.59 kcal/mole) A) Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 20-fold dilution of your pure protein in solution (by this, we mean that 50 ul of the protein sample was diluted to a final volume of 1 ml) and find A280 = 0.40. What is the original concentration of the protein before dilution? B) What is the concentration of the unfolded form of the protein in your sample?